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  1. 41

    Structural characterization of HDAC2-MTA1 complex by Narayan Gautam, Narayan Prasad Adhikari

    Published 2025-05-01
    “… Histone deacetylases are recruited to specific transcriptional repression complexes through interactions with corepressor proteins. …”
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    Article
  2. 42

    Structural features of somatic and germline retrotransposition events in humans by Päivi Nummi, Tatiana Cajuso, Tuukka Norri, Aurora Taira, Heli Kuisma, Niko Välimäki, Anna Lepistö, Laura Renkonen-Sinisalo, Selja Koskensalo, Toni T. Seppälä, Ari Ristimäki, Kyösti Tahkola, Anne Mattila, Jan Böhm, Jukka-Pekka Mecklin, Emma Siili, Annukka Pasanen, Oskari Heikinheimo, Ralf Bützow, Auli Karhu, Kathleen H. Burns, Kimmo Palin, Lauri A. Aaltonen

    Published 2025-04-01
    “…Moreover, transposons are normally repressed through epigenetic silencing in healthy adult tissues but become derepressed in several human cancers, with high activity detected in colorectal cancer. …”
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  3. 43

    Structural proteomics defines a sequential priming mechanism for the progesterone receptor by Matthew D. Mann, Min Wang, Josephine C. Ferreon, Phoebe S. Tsoi, Michael P. Suess, Antrix Jain, Anna Malovannaya, Roberto Vera Alvarez, Bruce D. Pascal, Raj Kumar, Dean P. Edwards, Patrick R. Griffin

    Published 2025-05-01
    “…Our findings reveal selective CoR NR-box binding by PR and unique interaction surfaces between PR and CoRs during complex assembly, providing a structural basis for CoR sequential binding on PR. Antagonist-bound PR showed persistent CoR interactions, challenging the classical model of nuclear receptor activation and repression. …”
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    Article
  4. 44

    Structural basis for transcription activation through cooperative recruitment of MntR by Haoyuan Shi, Yu Fu, Vilmante Kodyte, Amelie Andreas, Ankita J. Sachla, Keikilani Miller, Ritu Shrestha, John D. Helmann, Arthur Glasfeld, Shivani Ahuja

    Published 2025-03-01
    “…Abstract Bacillus subtilis MntR is a dual regulatory protein that responds to heightened Mn2+ availability in the cell by both repressing the expression of uptake transporters and activating the expression of efflux proteins. …”
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  5. 45
  6. 46

    Structural basis for higher-order DNA binding by a bacterial transcriptional regulator. by Frederik Oskar Graversgaard Henriksen, Lan Bich Van, Ditlev Egeskov Brodersen, Ragnhild Bager Skjerning

    Published 2025-06-01
    “…Here, we show that the Xre-RES complex interacts specifically with a palindromic DNA repeat in the promoter in a 1:1 molar ratio, leading to transcriptional repression. We determine the 2.7 Å crystal structure of the protein-DNA complex, revealing an unexpected asymmetry in the interaction and suggesting the presence of a secondary binding site, which is supported by structural prediction of the binding to the intact promoter region. …”
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    Article
  7. 47

    Perturbation of chromatin structure globally affects localization and recruitment of splicing factors. by Ignacio E Schor, David Llères, Guillermo J Risso, Andrea Pawellek, Jernej Ule, Angus I Lamond, Alberto R Kornblihtt

    Published 2012-01-01
    “…In addition, a similar effect is observed after depletion of the heterochromatic protein HP1α, associated with repressive chromatin. We used advanced imaging approaches to analyze in detail both the structural organization of the speckle compartment and nuclear distribution of splicing factors, as well as studying direct interactions between splicing factors and their association with chromatin in vivo. …”
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    Article
  8. 48

    Anti-church Terror during the October Revolution Through the Prism of the Historiografy by S. LEONOV

    Published 2014-04-01
    “…Nevertheless, several key issues still remains disputable since they have never been properly explored, e.g. the directly goals of the Bolsheviks’ policy toward the Church and factors of anti-Church terror; relation of the terror “from above” (official/ government structures) to the one “from below”; attitudes of the majority of the rural and urban populations; numbers of repressed members of clergy and laity, etc. …”
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  9. 49

    CryoEM structure of the SLFN14 endoribonuclease reveals insight into RNA binding and cleavage by Justin Van Riper, Arleth O. Martinez-Claros, Lie Wang, Hannah E. Schneiderman, Sweta Maheshwari, Monica C. Pillon

    Published 2025-07-01
    “…Here, we reconstitute active full-length human SLFN14 and report a high-resolution cryoEM reconstruction of the SLFN14•RNA complex. The structure reveals a medallion-like architecture that shares structural homology with other SLFN family members. …”
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    Article
  10. 50

    Chromatin structure and gene transcription of recombinant p53 adenovirus vector within host by Duo Ning, Yuqing Deng, Simon Zhongyuan Tian

    Published 2025-02-01
    “…IntroductionThe recombinant human p53 adenovirus (Ad-p53) offers a promising approach for cancer therapy, yet its chromatin structure and effects on host chromatin organization and gene expression are not fully understood.MethodsIn this study, we employed in situ ChIA-PET to investigate the colorectal cancer cell line HCT116 with p53 knockout, comparing them to cells infected with the adenovirus-vector expressing p53. …”
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  11. 51

    The Impact of Polycomb Group Proteins on 3D Chromatin Structure and Environmental Stresses in Plants by Yali Liu, Suxin Xiao, Minqi Yang, Guangqin Guo, Yue Zhou

    Published 2025-03-01
    “…The two multi-subunit complexes, Polycomb Repressive Complex 1 and 2 (PRC1/2), act synergistically during development to maintain the gene silencing state among different species. …”
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  12. 52

    Structural basis for spermidine recognition and modulation of Acinetobacter baumannii multidrug efflux regulator AmvR by Na Wang, Xu Wang, Mengxiang Zhou, Qingsong Lu, Yaling Xu, Ying Wang, Haiyun Wang, Beibei Yang, Shibing He, Liuliu Xu, Jie Li, Honghua Ge, Jinming Ma

    Published 2025-05-01
    “…Here, we report the crystal structure of the AmvR protein bound to its physiological substrate, spermidine, thereby offering structural and functional insights into AmvR. …”
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  13. 53

    Structure-guided discovery of novel dUTPase inhibitors with anti-Nocardia activity by computational design by Zhi-Zheng Wang, Jun Weng, Jing Qi, Xin-Xin Fu, Ban-Bin Xing, Yang Hu, Chun-Hsiang Huang, Chin-Yu Chen, Zigong Wei

    Published 2024-12-01
    “…In this study, we discovered a series of novel NsdUTPase inhibitors to fight against Nocardia. The first crystal structure of NsdUTPase was released, and a structure-based computational design was performed. …”
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  14. 54
  15. 55

    In vivo structure profiling reveals human cytosolic and mitochondrial tRNA structurome and interactome in response to stress by Noah Peña, Yichen Hou, Christopher P. Watkins, Sihao Huang, Wen Zhang, Christopher D. Katanski, Tao Pan

    Published 2025-05-01
    “…We also identify cytosolic and mitochondrial tRNA structure and interaction changes upon arsenite treatment, a type of oxidative stress that induces translational reprogramming, which is consistent with global translation repression in both compartments. …”
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  16. 56

    Molecular and functional analyses of a maize autoactive NB-LRR protein identify precise structural requirements for activity. by Guan-Feng Wang, Jiabing Ji, Farid El-Kasmi, Jeffery L Dangl, Guri Johal, Peter J Balint-Kurti

    Published 2015-02-01
    “…We report systematic structural and functional analyses of Rp1 proteins in maize and N. benthamiana to characterize the molecular mechanism of NLR activation/auto-inhibition. …”
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  17. 57

    PcG-mediated higher-order chromatin structures modulate replication programs at the Drosophila BX-C. by Federica Lo Sardo, Chiara Lanzuolo, Federico Comoglio, Marco De Bardi, Renato Paro, Valerio Orlando

    Published 2013-01-01
    “…Polycomb group proteins (PcG) exert conserved epigenetic functions that convey maintenance of repressed transcriptional states, via post-translational histone modifications and high order structure formation. …”
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  20. 60

    Structural and functional study of YER067W, a new protein involved in yeast metabolism control and drug resistance. by Tatiana Domitrovic, Guennadi Kozlov, João Claudio Gonçalves Freire, Claudio Akio Masuda, Marcius da Silva Almeida, Mónica Montero-Lomeli, Georgia Correa Atella, Edna Matta-Camacho, Kalle Gehring, Eleonora Kurtenbach

    Published 2010-06-01
    “…As the majority of these ORFs have no homologs with characterized sequence or protein structure, traditional sequence-based approaches cannot be applied to deduce their biological function. …”
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